Header list of 1nmw.pdb file
Complete list - r 25 2 Bytes
HEADER ISOMERASE 12-JAN-03 1NMW
TITLE SOLUTION STRUCTURE OF THE PPIASE DOMAIN OF HUMAN PIN1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PPIASE DOMAIN (RESIDUES 50-163);
COMPND 5 SYNONYM: ROTAMASE PIN1, PPIASE PIN1;
COMPND 6 EC: 5.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PIN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PPIASE DOMAIN, BETA-ALPHA, A1/B1 LOOP, SULPHATE, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR E.BAYER,S.GOETTSCH,J.W.MUELLER,B.GRIEWEL,E.GUIBERMAN,L.MAYR,P.BAYER
REVDAT 3 09-MAR-11 1NMW 1 REMARK
REVDAT 2 24-FEB-09 1NMW 1 VERSN
REVDAT 1 15-JUL-03 1NMW 0
JRNL AUTH E.BAYER,S.GOETTSCH,J.W.MUELLER,B.GRIEWEL,E.GUIBERMAN,
JRNL AUTH 2 L.M.MAYR,P.BAYER
JRNL TITL STRUCTURAL ANALYSIS OF THE MITOTIC REGULATOR HPIN1 IN
JRNL TITL 2 SOLUTION: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE
JRNL TITL 3 BINDING.
JRNL REF J.BIOL.CHEM. V. 278 26183 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12721297
JRNL DOI 10.1074/JBC.M300721200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.P.LU,S.D.HANNES,T.HUNTER
REMARK 1 TITL A HUMAN PEPTIDYL-PROLYL ISOMERASE ESSENTIAL FOR REGULATION
REMARK 1 TITL 2 OF MITOSIS
REMARK 1 REF NATURE V. 380 544 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/380544A0
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.RANGANATHAN,K.P.LU,T.HUNTER,J.P.NOEL
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE MITOTIC ROTAMASE
REMARK 1 TITL 2 PIN1 SUGGESTS SUBSTRATE RECOGNITION IS PHOSPHORYLATION
REMARK 1 TITL 3 DEPENDENT
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 89 875 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80273-1
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.A.VERDECIA,M.E.BOWMAN,K.P.LU,T.HUNTER,J.P.NOEL
REMARK 1 TITL STRUCTURAL BASIS FOR PHOSPHOSERINE-PROLINE RECOGNITION BY
REMARK 1 TITL 2 GROUP IV WW DOMAINS
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 639 2000
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/77929
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUENGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-03.
REMARK 100 THE RCSB ID CODE IS RCSB018017.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300; 300
REMARK 210 PH : 6.6; 6.6; 6.6; 6.6
REMARK 210 IONIC STRENGTH : N.C.; N.C.; N.C.; N.C.
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6-0.8MM PIN1(PPIASE) U-15N,
REMARK 210 13C; 50MM PHOSPHATE BUFFER, 1MM
REMARK 210 DTT, 5MM EDTA, 50-100MM NA
REMARK 210 SULPHATE; ~0.1-0.2MM PIN1(PPIAS)
REMARK 210 U-15N,13C; 50MM PHOSPHATE BUFFER,
REMARK 210 1MM DTT, 5MM EDTA, 50-100MM NA
REMARK 210 SULPHATE; 0.6-0.8MM PIN1(PPIASE)
REMARK 210 U-15N,13C;50MM TRIS/HCL BUFFER,
REMARK 210 1MM DTT, 5MM EDTA; 0.8MM
REMARK 210 PIN1(PPIASE); 50MM PHOSPHATE
REMARK 210 BUFFER, 1MM DTT, 5MM EDTA, 50-
REMARK 210 100MM NA SULPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY;
REMARK 210 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.2, AURELIA 2.8.11,
REMARK 210 VNMR 6.18, NDEE 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: HYDROGEN BONDS WERE EXTRACTED FROM HSQC SPECTRA IN D2O
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H THR A 152 O GLY A 155 1.59
REMARK 500 O GLU A 135 H PHE A 139 1.61
REMARK 500 H SER A 147 O ILE A 159 1.63
REMARK 500 H SER A 72 O GLN A 75 1.66
REMARK 500 O ASP A 102 H LEU A 106 1.67
REMARK 500 O LEU A 86 H ASN A 90 1.67
REMARK 500 O VAL A 150 H HIS A 157 1.68
REMARK 500 O THR A 81 H ALA A 85 1.69
REMARK 500 O ALA A 107 H SER A 111 1.69
REMARK 500 H SER A 65 O ARG A 80 1.70
REMARK 500 O PHE A 134 H SER A 138 1.73
REMARK 500 O ARG A 69 H SER A 71 1.74
REMARK 500 O SER A 58 H LEU A 160 1.76
REMARK 500 O ARG A 56 H THR A 162 1.77
REMARK 500 O PHE A 103 H ALA A 107 1.81
REMARK 500 H SER A 58 O LEU A 160 1.88
REMARK 500 O VAL A 55 H PHE A 125 1.92
REMARK 500 H VAL A 150 O HIS A 157 1.93
REMARK 500 O PRO A 70 H ILE A 78 1.94
REMARK 500 H LEU A 60 O ILE A 158 1.94
REMARK 500 HE1 TRP A 73 O CYS A 113 1.94
REMARK 500 O SER A 115 H GLY A 120 1.95
REMARK 500 O LYS A 82 H LEU A 86 1.95
REMARK 500 O SER A 115 H ALA A 118 1.96
REMARK 500 HA HIS A 59 O ILE A 158 1.97
REMARK 500 O ALA A 116 H ARG A 119 1.97
REMARK 500 O ILE A 89 H ILE A 93 1.99
REMARK 500 O ASN A 90 H GLN A 94 1.99
REMARK 500 O ILE A 93 H LYS A 97 2.00
REMARK 500 O GLN A 94 H SER A 98 2.01
REMARK 500 OG SER A 154 HE2 HIS A 157 2.04
REMARK 500 O LYS A 132 H ASP A 136 2.05
REMARK 500 OD2 ASP A 102 H SER A 105 2.05
REMARK 500 O ALA A 107 H PHE A 110 2.05
REMARK 500 O GLU A 104 HB3 ARG A 119 2.06
REMARK 500 O GLU A 83 H GLU A 87 2.06
REMARK 500 O ASP A 136 H ALA A 140 2.08
REMARK 500 O LEU A 88 H TYR A 92 2.08
REMARK 500 H VAL A 55 O PHE A 125 2.09
REMARK 500 H GLY A 144 O ARG A 161 2.09
REMARK 500 O PHE A 134 HB2 SER A 138 2.11
REMARK 500 O PRO A 133 H ALA A 137 2.11
REMARK 500 H VAL A 62 O ILE A 156 2.12
REMARK 500 O GLU A 135 HB2 PHE A 139 2.12
REMARK 500 O ILE A 96 H GLY A 99 2.12
REMARK 500 O HIS A 64 H SER A 67 2.13
REMARK 500 O GLU A 145 HA LEU A 160 2.13
REMARK 500 O SER A 58 HA ILE A 159 2.14
REMARK 500 O SER A 114 H LYS A 117 2.16
REMARK 500 HG3 ARG A 54 O PHE A 125 2.17
REMARK 500
REMARK 500 THIS ENTRY HAS 571 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 52 -174.47 -67.77
REMARK 500 1 ARG A 69 88.63 -152.56
REMARK 500 1 PRO A 70 63.49 -68.84
REMARK 500 1 GLN A 131 151.02 -47.99
REMARK 500 2 ARG A 69 84.02 -156.75
REMARK 500 2 GLU A 76 -45.63 -133.77
REMARK 500 2 SER A 114 1.68 -61.84
REMARK 500 2 ASP A 153 -52.38 -24.12
REMARK 500 2 THR A 162 -67.63 -99.48
REMARK 500 3 ARG A 69 83.44 -153.03
REMARK 500 3 ARG A 80 95.30 -56.52
REMARK 500 3 ASP A 112 44.02 -90.74
REMARK 500 3 SER A 114 1.22 -61.69
REMARK 500 4 GLU A 51 50.90 -156.54
REMARK 500 4 ARG A 69 85.77 -154.58
REMARK 500 4 PRO A 70 89.78 -68.97
REMARK 500 4 SER A 71 -161.10 -178.97
REMARK 500 4 ARG A 74 31.40 -99.56
REMARK 500 4 GLN A 75 -142.27 75.43
REMARK 500 4 GLU A 76 126.77 61.50
REMARK 500 4 THR A 79 50.43 -159.97
REMARK 500 4 ASP A 102 151.93 -44.30
REMARK 500 4 ASP A 112 35.38 -91.48
REMARK 500 4 ALA A 116 -32.95 -37.61
REMARK 500 4 ASP A 121 99.98 -59.42
REMARK 500 5 GLU A 51 88.51 64.05
REMARK 500 5 ARG A 69 87.87 -151.40
REMARK 500 5 PRO A 70 68.20 -67.00
REMARK 500 5 SER A 114 0.27 -64.06
REMARK 500 5 ARG A 119 31.37 75.99
REMARK 500 5 ASP A 121 104.49 -56.91
REMARK 500 5 ARG A 127 104.59 -50.35
REMARK 500 5 THR A 162 -61.78 -99.46
REMARK 500 6 ARG A 69 84.32 -153.67
REMARK 500 6 SER A 71 145.37 -172.97
REMARK 500 6 ASP A 102 157.13 -48.19
REMARK 500 6 SER A 114 0.38 -63.43
REMARK 500 6 ASP A 121 99.98 -56.01
REMARK 500 7 ARG A 69 81.31 -151.05
REMARK 500 7 ASP A 112 33.93 -91.31
REMARK 500 8 SER A 114 0.26 -63.08
REMARK 500 8 ASP A 121 105.38 -52.76
REMARK 500 8 GLN A 131 159.22 -45.99
REMARK 500 8 ASP A 153 -39.91 -38.74
REMARK 500 9 THR A 79 50.75 -150.24
REMARK 500 9 THR A 81 174.71 -56.55
REMARK 500 9 ASP A 102 159.56 -45.69
REMARK 500 9 ALA A 116 -33.26 -39.62
REMARK 500 9 THR A 162 -60.48 -99.43
REMARK 500 10 GLU A 51 167.73 60.94
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NMV RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN PIN1
REMARK 900 RELATED ID: 1PIN RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HPIN1 WITH ALA-PRO PEPTIDE COMPLEXED TO
REMARK 900 PPIASE DOMAIN
REMARK 900 RELATED ID: 1F8A RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HPIN1 WITH CTD PEPTIDE COMPLEXED TO WW
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1EQ3 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN PARVULIN14
REMARK 900 RELATED ID: 5305 RELATED DB: BMRB
REMARK 900 ASSIGNMENTS OF HPIN1
DBREF 1NMW A 50 163 UNP Q13526 PIN1_HUMAN 50 163
SEQRES 1 A 114 GLY GLU PRO ALA ARG VAL ARG CYS SER HIS LEU LEU VAL
SEQRES 2 A 114 LYS HIS SER GLN SER ARG ARG PRO SER SER TRP ARG GLN
SEQRES 3 A 114 GLU LYS ILE THR ARG THR LYS GLU GLU ALA LEU GLU LEU
SEQRES 4 A 114 ILE ASN GLY TYR ILE GLN LYS ILE LYS SER GLY GLU GLU
SEQRES 5 A 114 ASP PHE GLU SER LEU ALA SER GLN PHE SER ASP CYS SER
SEQRES 6 A 114 SER ALA LYS ALA ARG GLY ASP LEU GLY ALA PHE SER ARG
SEQRES 7 A 114 GLY GLN MET GLN LYS PRO PHE GLU ASP ALA SER PHE ALA
SEQRES 8 A 114 LEU ARG THR GLY GLU MET SER GLY PRO VAL PHE THR ASP
SEQRES 9 A 114 SER GLY ILE HIS ILE ILE LEU ARG THR GLU
HET SO4 A 200 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
HELIX 1 1 THR A 81 SER A 98 1 18
HELIX 2 2 ASP A 102 SER A 111 1 10
HELIX 3 3 CYS A 113 ARG A 119 5 7
HELIX 4 4 GLN A 131 LEU A 141 1 11
SHEET 1 A 4 ASP A 121 SER A 126 0
SHEET 2 A 4 ARG A 54 VAL A 62 -1 N VAL A 55 O PHE A 125
SHEET 3 A 4 ILE A 156 ARG A 161 -1 O LEU A 160 N SER A 58
SHEET 4 A 4 VAL A 150 PHE A 151 -1 N VAL A 150 O HIS A 157
SITE 1 AC1 4 LYS A 63 ARG A 68 ARG A 69 SER A 154
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 25 2 Bytes